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Levels and location of adenosine 5′-triphosphate in bovine milk

Published online by Cambridge University Press:  01 June 2009

Thomas Richardson
Affiliation:
The Agricultural Institute, Moorepark Research Centre, Fermoy, Co. Cork, Irish Republic
Thomas C. A. McGann
Affiliation:
The Agricultural Institute, Moorepark Research Centre, Fermoy, Co. Cork, Irish Republic
Robert D. Kearney
Affiliation:
The Agricultural Institute, Moorepark Research Centre, Fermoy, Co. Cork, Irish Republic

Summary

Bovine milk systems were analysed for adenosine 5′-triphosphate (ATP) using the luciferase-ATP reaction in a liquid scintillation counter. Approximately 0·2 µmol ATP/1 milk serum were evident both in whole milks and the corresponding skim-milks. ATP was not detectable in skim-milk ultrafiltrates. These findings indicated that ATP was present in a non-dialysable portion of skim-milk. Centri-fugation of whole milks from individual cows at 5500 g for 15 min at 10°C yielded skim-milks essentially devoid of somatic cells and bacteria. However, the ATP in the skim-milks decreased by less than 20% compared with the whole milks indicating that the calcium phosphate-citrate (CPC)–caseinate micelles were the source of the ATP. ATP was not detectable in colloidal phosphate-free milk, from which CPC had been removed, confirming that the ATP was sequestered in the constituent CPC. Likewise, the occurrence of significant amounts of Mg, another potent stabilizer of amorphous calcium phosphate (ACP) in other biological systems, was confirmed in the colloidal phosphate of milk. From 0·13 to 0·31 µmole ATP/1 (mean, 0·23) was found in the 9 milk samples studied. The discovery of small but appreciable levels of ATP in the CPC of milk provides further evidence for the analogy previously shown to exist between the CPC complex of milk and the ACP which accumulates in mitochondria. The latter has been postulated to provide an essential precursor for crystalline bone salts to form in ordered calcification processes. The implications of these findings in the biosynthesis of milk are briefly discussed.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1980

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References

REFERENCES

Anon, . (1976). Standard conditions for calcium and magnesium. In Analytical Methods for Atomic Absorption Spectrophotometry. Norwalk, Conn.: Perkin-Elmer Corp.Google Scholar
Armstrong, W. D. & Singer, L. (1965). Clinical Orthopaedics 38, 179190.Google Scholar
Baumrucker, C. R. & Keenan, T. W. (1975). Experimental Cell Research 90, 253260.Google Scholar
Becker, G. L., Chen, C. H., Greenawalt, J. W. & Lehninger, A. L. (1974). Journal of Cell Biology 61, 316326.Google Scholar
Bizar, S., Felix, R., Neuman, W. F. & Fleisch, H. (1978). Mineral and Electrolyte Metabolism 1, 7483.Google Scholar
Brazis, A. R., Jasper, D. E., Levowitz, D., Newbould, F. H. S., Postle, D. S., Schultze, W. D., Smith, J. W. & Ullmann, W. W. (1968). Journal of Milk and Food Technology 31, 350354.Google Scholar
Brunner, J. R. (1974). In Fundamentals of Dairy Chemistry, 2nd edn, p. 536. (Eds Webb, B. H., Johnson, A. H. & Alford, J. A..) Westport, Conn.: Avi Publishing Co.Google Scholar
Carafoli, E., Rossi, C. S. & Lehninger, A. L. (1965). Journal of Biological Chemistry 240, 22542261.Google Scholar
Emerson, C. P. Jr & Humphreys, T. (1971). Analytical Biochemistry 40, 254266.CrossRefGoogle Scholar
Fiske, C. H. & Subbarow, Y. (1925). Journal of Biological Chemistry 66, 375400.Google Scholar
Hausler, W. J. Jr (Ed.) (1972). Standard Methods for the Examination of Dairy Products, 13th edn.New York: American Public Health Association.Google Scholar
Johnson, A. H. (1974). In Fundamentals of Dairy Chemistry, 2nd edn, p. 31. (Eds Webb, B. H., Johnson, A. H. & Alford, J. A..) Westport, Conn.: Avi Publishing Co.Google Scholar
Kay, H. D. & Marshall, P. G. (1928). Biochemical Journal 22, 416418.Google Scholar
Krane, S. M. & Glimcher, M. L. (1962). Journal of Biological Chemistry 237, 29912998.Google Scholar
Kuyper, A. C. (1938). Journal of Biological Chemistry 123, 405407.Google Scholar
Lehninger, A. L. (1977). Horizons in Biochemistry and Biophysics 4, 130.Google Scholar
Lehninger, A. L., Reynafarje, B., Veroesi, A. & Tew, W. P. (1978). Annals of the New York Academy of Sciences 307, 160174.Google Scholar
Linzell, J. L., Mepham, T. B. & Peaker, M. (1976). Journal of Physiology 260, 739750.Google Scholar
McGann, T. C. A. (1960). Journal of Bone and Joint Surgery 42–B, 855856 (Abstract).Google Scholar
McGann, T. C. A. (1979). Biochemical Society Transactions 7, 5152.CrossRefGoogle Scholar
McGann, T. C. A., Kearney, R. D. & Donnelly, W. J. (1979). Journal of Dairy Research 46, 307311.CrossRefGoogle Scholar
McGann, T. C. A. & Pyne, G. T. (1960). Journal of Dairy Research 27, 403417.Google Scholar
Posner, A. S. (1978). Annals of the New York Academy of Sciences 307, 248249.CrossRefGoogle Scholar
Pyne, G. T. & McGann, T. C. A. (1960). Journal of Dairy Research 27, 916.CrossRefGoogle Scholar
Rubin, M. (1963). In The Transfer of Calcium and Strontium Across Biological Membranes, p. 33. (Ed. Wasserman, R. H..) New York: Academic Press.Google Scholar
Sutor, D. J., Percival, J. M. & Doonan, S. (1978). Clinica Chimica Acta 89, 273278.Google Scholar
Van Der Have, A. J. (1954). Netherlands Milk and Dairy Journal 8, 157162.Google Scholar